ID DEK_HUMAN Reviewed; 375 AA. AC P35659; B2R6K6; B4DN37; Q5TGV4; Q5TGV5; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 02-SEP-2026, entry version 224. DE RecName: Full=Protein DEK; GN Name=DEK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH RP NUP214, AND INVOLVEMENT IN ACUTE MYELOID LEUKEMIA. RC TISSUE=Testis; RX PubMed=1549122; DOI=10.1128/mcb.12.4.1687-1697.1992; RA Von Lindern M., Fornerod M., Van Baal S., Jaegle M., De Wit T., Buijs A., RA Grosveld G.; RT "The translocation (6;9), associated with a specific subtype of acute RT myeloid leukemia, results in the fusion of two genes, dek and can, and the RT expression of a chimeric, leukemia-specific dek-can mRNA."; RL Mol. Cell. Biol. 12:1687-1697(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 2-21; 66-84; 94-100; 112-124; 126-137; 169-177; RP 179-187; 331-344 AND 349-362, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION RP AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [7] RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) RP WITH RBM8A; RNPS1; SRRM1 AND ALYREF/THOC4. RX PubMed=11118221; DOI=10.1093/emboj/19.24.6860; RA Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.; RT "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of RT mRNA exon-exon junctions."; RL EMBO J. 19:6860-6869(2000). RN [8] RP INTERACTION WITH DAXX. RX PubMed=12140263; DOI=10.1242/jcs.115.16.3319; RA Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.; RT "Daxx and histone deacetylase II associate with chromatin through an RT interaction with core histones and the chromatin-associated protein Dek."; RL J. Cell Sci. 115:3319-3330(2002). RN [9] RP PHOSPHORYLATION AT SER-32; SER-159; THR-199; SER-201; SER-204; SER-243; RP SER-244; SER-251; SER-287; SER-288; THR-289; THR-290; SER-296; SER-301; RP SER-303; SER-306 AND SER-307. RX PubMed=15199154; DOI=10.1128/mcb.24.13.6011-6020.2004; RA Kappes F., Damoc C., Knippers R., Przybylski M., Pinna L.A., Gruss C.; RT "Phosphorylation by protein kinase CK2 changes the DNA binding properties RT of the human chromatin protein DEK."; RL Mol. Cell. Biol. 24:6011-6020(2004). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-51; SER-227; SER-230; RP SER-231 AND SER-232, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP IDENTIFICATION IN THE B-WICH COMPLEX. RX PubMed=16603771; DOI=10.1074/jbc.m600233200; RA Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.; RT "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear RT proteins in transcription."; RL J. Biol. Chem. 281:16264-16271(2006). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17524367; DOI=10.1016/j.bbrc.2007.05.019; RA Hu H.G., Scholten I., Gruss C., Knippers R.; RT "The distribution of the DEK protein in mammalian chromatin."; RL Biochem. Biophys. Res. Commun. 358:1008-1014(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP SUBCELLULAR LOCATION. RX PubMed=19695025; DOI=10.1111/j.1365-2443.2009.01324.x; RA Takata H., Nishijima H., Ogura S., Sakaguchi T., Bubulya P.A., RA Mochizuki T., Shibahara K.; RT "Proteome analysis of human nuclear insoluble fractions."; RL Genes Cells 14:975-990(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT THR-13; SER-19; SER-32; SER-51; SER-210; SER-230; SER-231; RP SER-232; SER-306 AND SER-307, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT THR-13; SER-32; SER-51; SER-301; SER-303; SER-306 AND SER-307, RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-32; SER-51; SER-72; RP SER-121; SER-122; SER-301; SER-306 AND SER-307, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-231; SER-232; RP SER-301; SER-303; SER-306 AND SER-307, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [24] RP ADP-RIBOSYLATION AT SER-279. RX PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003; RA Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I., RA Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.; RT "Serine ADP-ribosylation depends on HPF1."; RL Mol. Cell 0:0-0(2017). RN [25] RP STRUCTURE BY NMR OF 309-375, AND DNA-BINDING. RX PubMed=15238633; DOI=10.1110/ps.04797104; RA Devany M., Kotharu N.P., Matsuo H.; RT "Solution NMR structure of the C-terminal domain of the human protein RT DEK."; RL Protein Sci. 13:2252-2259(2004). RN [26] RP STRUCTURE BY NMR OF 78-208, AND DNA-BINDING. RX PubMed=18227428; DOI=10.1110/ps.073244108; RA Devany M., Kappes F., Chen K.M., Markovitz D.M., Matsuo H.; RT "Solution NMR structure of the N-terminal domain of the human DEK RT protein."; RL Protein Sci. 17:205-215(2008). CC -!- FUNCTION: Involved in chromatin organization. CC {ECO:0000269|PubMed:17524367}. CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex (EJC) CC with DEK, RBM8A, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with histones CC H2A, H2B, H3, H4, acetylated histone H4, non-phosphorylated DAXX and CC HDAC2. Component of the B-WICH complex, at least composed of CC SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. CC Binds DNA. {ECO:0000269|PubMed:11118221, ECO:0000269|PubMed:12140263, CC ECO:0000269|PubMed:16603771}. CC -!- INTERACTION: CC P35659; P68400: CSNK2A1; NbExp=3; IntAct=EBI-301977, EBI-347804; CC P35659; Q8N954-2: GPATCH11; NbExp=3; IntAct=EBI-301977, EBI-12178961; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17524367, CC ECO:0000269|PubMed:19695025}. Note=Enriched in regions where chromatin CC is decondensed or sparse in the interphase nuclei. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P35659-1; Sequence=Displayed; CC Name=2; CC IsoId=P35659-2; Sequence=VSP_042951; CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at relatively high levels. CC -!- PTM: Phosphorylated by CK2. Phosphorylation fluctuates during the cell CC cycle with a moderate peak during G(1) phase, and weakens the binding CC of DEK to DNA. {ECO:0000269|PubMed:15199154}. CC -!- DISEASE: Note=A chromosomal aberration involving DEK is found in a CC subset of acute myeloid leukemia (AML); also known as acute non- CC lymphocytic leukemia (PubMed:1549122). Translocation t(6;9)(p23;q34) CC with NUP214/CAN (PubMed:1549122). It results in the formation of a DEK- CC NUP214 fusion gene (PubMed:1549122). {ECO:0000269|PubMed:1549122}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/23/DEK"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X64229; CAA45536.1; -; mRNA. DR EMBL; AK297749; BAG60099.1; -; mRNA. DR EMBL; AK312616; BAG35503.1; -; mRNA. DR EMBL; AL031774; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471087; EAW55402.1; -; Genomic_DNA. DR EMBL; BC035259; AAH35259.1; -; mRNA. DR CCDS; CCDS34344.1; -. [P35659-1] DR CCDS; CCDS47382.1; -. [P35659-2] DR PIR; S26059; S26059. DR RefSeq; NP_001128181.1; NM_001134709.2. [P35659-2] DR RefSeq; NP_003463.1; NM_003472.4. [P35659-1] DR RefSeq; XP_024302312.1; XM_024446544.2. [P35659-1] DR RefSeq; XP_054212352.1; XM_054356377.1. [P35659-1] DR PDB; 1Q1V; NMR; -; A=309-375. DR PDB; 2JX3; NMR; -; A=78-208. DR PDB; 8KCY; EM; 2.80 A; K/L=1-375. DR PDB; 8KD1; EM; 3.20 A; K=1-375. DR PDB; 9L1X; EM; 2.69 A; K/L=1-375. DR PDB; 9L22; EM; 3.00 A; K/L=1-375. DR AlphaFoldDB; P35659; -. DR BMRB; P35659; -. DR EMDB; EMD-37115; -. DR EMDB; EMD-37121; -. DR EMDB; EMD-62757; -. DR EMDB; EMD-62766; -. DR MDposit; P35659; -. DR SMR; P35659; -. DR BioGRID; 113643; 227. DR ComplexPortal; CPX-1099; B-WICH chromatin remodelling complex. DR CORUM; P35659; -. DR FunCoup; P35659; 3400. DR IntAct; P35659; 69. DR MINT; P35659; -. DR NDEx; IQUERY-CP-DEK; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000498653; -. DR BindingDB; P35659; -. DR ChEMBL; CHEMBL6066180; -. DR GlyGen; P35659; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P35659; -. DR MetOSite; P35659; -. DR PhosphoSitePlus; P35659; -. DR SwissPalm; P35659; -. DR BioMuta; DEK; -. DR DMDM; 544150; -. DR jPOST; P35659; -. DR MassIVE; P35659; -. DR PaxDb; 9606-ENSP00000498653; -. DR PeptideAtlas; P35659; -. DR ProteomicsDB; 55127; -. [P35659-1] DR ProteomicsDB; 55128; -. [P35659-2] DR Pumba; P35659; -. DR Antibodypedia; 4456; 309 antibodies from 40 providers. DR DNASU; 7913; -. DR Ensembl; ENST00000244776.11; ENSP00000244776.7; ENSG00000124795.18. [P35659-2] DR Ensembl; ENST00000652576.1; ENSP00000498335.1; ENSG00000124795.18. [P35659-1] DR Ensembl; ENST00000652689.1; ENSP00000498653.1; ENSG00000124795.18. [P35659-1] DR Ensembl; ENST00000852492.1; ENSP00000522551.1; ENSG00000124795.18. [P35659-1] DR Ensembl; ENST00000852493.1; ENSP00000522552.1; ENSG00000124795.18. [P35659-2] DR Ensembl; ENST00000919563.1; ENSP00000589622.1; ENSG00000124795.18. [P35659-1] DR GeneID; 7913; -. DR KEGG; hsa:7913; -. DR MANE-Select; ENST00000652689.1; ENSP00000498653.1; NM_003472.4; NP_003463.1. DR UCSC; uc003ncr.2; human. [P35659-1] DR AGR; HGNC:2768; -. DR ClinPGx; PA27251; -. DR CTD; 7913; -. DR DisGeNET; 7913; -. DR GeneCards; DEK; -. DR HGNC; HGNC:2768; DEK. DR HPA; ENSG00000124795; Low tissue specificity. DR MalaCards; DEK; -. DR MIM; 125264; gene. DR OpenTargets; ENSG00000124795; -. DR Orphanet; 402014; Acute myeloid leukemia with t(6;9)(p23;q34). DR VEuPathDB; HostDB:ENSG00000124795; -. DR eggNOG; KOG2266; Eukaryota. DR GeneTree; ENSGT00390000017282; -. DR HOGENOM; CLU_041060_0_1_1; -. DR InParanoid; P35659; -. DR OMA; MIKKAPT; -. DR OrthoDB; 370884at2759; -. DR PAN-GO; P35659; 3 GO annotations based on evolutionary models. DR PhylomeDB; P35659; -. DR PathwayCommons; P35659; -. DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-HSA-8864260; Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors. DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis. DR SignaLink; P35659; -. DR SIGNOR; P35659; -. DR Agora; ENSG00000124795; -. DR BioGRID-ORCS; 7913; 98 hits in 1173 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR ChiTaRS; DEK; human. DR EvolutionaryTrace; P35659; -. DR GeneWiki; DEK_(gene); -. DR GenomeRNAi; 7913; -. DR Pharos; P35659; Tbio. DR PRO; PR:P35659; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P35659; protein. DR Bgee; ENSG00000124795; Expressed in calcaneal tendon and 207 other cell types or tissues. DR ExpressionAtlas; P35659; baseline and differential. DR GO; GO:0110016; C:B-WICH complex; IDA:ComplexPortal. DR GO; GO:0043292; C:contractile muscle fiber; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; NAS:ComplexPortal. DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:ComplexPortal. DR GO; GO:2000779; P:regulation of double-strand break repair; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR GO; GO:0019079; P:viral genome replication; TAS:ProtInc. DR FunFam; 1.10.10.60:FF:000148; Dek, isoform B; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR InterPro; IPR044198; DEK. DR InterPro; IPR014876; DEK_C. DR InterPro; IPR003034; SAP_dom. DR PANTHER; PTHR13468; DEK PROTEIN; 1. DR PANTHER; PTHR13468:SF1; PROTEIN DEK; 1. DR Pfam; PF08766; DEK_C; 1. DR Pfam; PF02037; SAP; 1. DR SMART; SM00513; SAP; 1. DR SUPFAM; SSF109715; DEK C-terminal domain; 1. DR PROSITE; PS51998; DEK_C; 1. DR PDBsum; 1Q1V; -. DR PDBsum; 2JX3; -. DR PDBsum; 8KCY; -. DR PDBsum; 8KD1; -. DR PDBsum; 9L1X; -. DR PDBsum; 9L22; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing; KW Chromatin regulator; Chromosomal rearrangement; Direct protein sequencing; KW DNA-binding; Nucleus; Phosphoprotein; Proteomics identification; KW Proto-oncogene; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..375 FT /note="Protein DEK" FT /id="PRO_0000079858" FT DOMAIN 149..183 FT /note="SAP" FT DOMAIN 319..375 FT /note="DEK-C" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342" FT DNA_BIND 337..351 FT DNA_BIND 367..371 FT REGION 1..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 184..325 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 205..221 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 19..30 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 31..47 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 48..61 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 194..203 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 243..253 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 258..277 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 278..296 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:22814378" FT MOD_RES 13 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 15 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q6AXS3" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 32 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 51 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 72 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 121 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 122 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 159 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 199 FT /note="Phosphothreonine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 201 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 204 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 210 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 227 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 230 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT MOD_RES 231 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT MOD_RES 243 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 244 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 251 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 279 FT /note="ADP-ribosylserine" FT /evidence="ECO:0000269|PubMed:28190768" FT MOD_RES 287 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 288 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 289 FT /note="Phosphothreonine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 290 FT /note="Phosphothreonine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 296 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154" FT MOD_RES 301 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 303 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 306 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 307 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15199154, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 49..82 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042951" FT VARIANT 140 FT /note="V -> A (in dbSNP:rs17336208)" FT /id="VAR_050949" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:9L22" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:8KD1" FT HELIX 63..66 FT /evidence="ECO:0007829|PDB:9L1X" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:9L1X" FT HELIX 92..100 FT /evidence="ECO:0007829|PDB:9L1X" FT HELIX 103..114 FT /evidence="ECO:0007829|PDB:9L1X" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:9L1X" FT HELIX 120..128 FT /evidence="ECO:0007829|PDB:9L1X" FT HELIX 140..150 FT /evidence="ECO:0007829|PDB:9L1X" FT HELIX 154..163 FT /evidence="ECO:0007829|PDB:9L1X" FT HELIX 172..184 FT /evidence="ECO:0007829|PDB:9L1X" FT HELIX 319..321 FT /evidence="ECO:0007829|PDB:1Q1V" FT HELIX 322..333 FT /evidence="ECO:0007829|PDB:1Q1V" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:1Q1V" FT HELIX 343..353 FT /evidence="ECO:0007829|PDB:1Q1V" FT STRAND 355..357 FT /evidence="ECO:0007829|PDB:1Q1V" FT HELIX 361..375 FT /evidence="ECO:0007829|PDB:1Q1V" SQ SEQUENCE 375 AA; 42674 MW; C07D22B37B719A23 CRC64; MSASAPAAEG EGTPTQPASE KEPEMPGPRE ESEEEEDEDD EEEEEEEKEK SLIVEGKREK KKVERLTMQV SSLQREPFTI AQGKGQKLCE IERIHFFLSK KKTDELRNLH KLLYNRPGTV SSLKKNVGQF SGFPFEKGSV QYKKKEEMLK KFRNAMLKSI CEVLDLERSG VNSELVKRIL NFLMHPKPSG KPLPKSKKTC SKGSKKERNS SGMARKAKRT KCPEILSDES SSDEDEKKNK EESSDDEDKE SEEEPPKKTA KREKPKQKAT SKSKKSVKSA NVKKADSSTT KKNQNSSKKE SESEDSSDDE PLIKKLKKPP TDEELKETIK KLLASANLEE VTMKQICKKV YENYPTYDLT ERKDFIKTTV KELIS //